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Crystallization and preliminary X-ray analysis of Escherichia coli RNase G.

ABSTRACT: The homologous RNases RNase E and RNase G are widely distributed in bacteria and function in many important physiological processes, including mRNA degradation, rRNA maturation and so on. In this study, the crystallization and preliminary X-ray analysis of RNase G from Escherichia coli is described. Purified recombinant E. coli RNase G, which has 497 amino acids, was crystallized in the cubic space group F432, with unit-cell parameters a = b = c = 219.84 A. X-ray diffraction data were collected to a resolution of 3.4 A.

SUBMITTER: Fang P

PROVIDER: S-EPMC2688416 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of Escherichia coli RNase G.

Fang Pengfei P Wang Jing J Li Xu X Guo Min M Xing Li L Cao Xu X Zhu Yi Y Gao Yan Y Niu Liwen L Teng Maikun M

Acta crystallographica. Section F, Structural biology and crystallization communications 20090522 Pt 6

The homologous RNases RNase E and RNase G are widely distributed in bacteria and function in many important physiological processes, including mRNA degradation, rRNA maturation and so on. In this study, the crystallization and preliminary X-ray analysis of RNase G from Escherichia coli is described. Purified recombinant E. coli RNase G, which has 497 amino acids, was crystallized in the cubic space group F432, with unit-cell parameters a = b = c = 219.84 A. X-ray diffraction data were collected ...[more]

PMID: 19478437

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